scholarly journals Sperm-associated seminal plasma proteins - a novel approach for the evaluation of sperm fertilizing ability of stallions?

1999 ◽  
Vol 15 (6) ◽  
pp. 531-537 ◽  
Author(s):  
A Reineke ◽  
Heß,O ◽  
A Schambony ◽  
A M Petrounkina ◽  
H Bader ◽  
...  
Reproduction ◽  
2021 ◽  
Author(s):  
Arabela Guedes de Azevedo Viana ◽  
Iara Magalhães Ribeiro ◽  
Renner Philipe Rodrigues Carvalho ◽  
Erdogan Memili ◽  
Arlindo Alencar Moura ◽  
...  

Proteomic approaches have been widely used in reproductive studies to uncover protein biomarkers of bull fertility. Seminal plasma is one of the most relevant sources of these proteins that may influence sperm physiology. Nonetheless, there are still gaps in existing knowledge in the functional attributes of seminal proteins. Thus, we reviewed the relationships between seminal plasma proteins and bull fertility by conducting a systematic review with data obtained from 71 studies. This review showed that the associations between fertility improvement with the use of total seminal plasma proteins are still controversial. None of the studies explored the sperm fertilizing ability following these interactions. By contrast, the exposure to a single protein, such as osteopontin, binder of sperm proteins, and heparin binding proteins, can increment sperm motility, capacitation, and fertilizing ability by modulating intracellular calcium concentrations, removing lipids from sperm membranes, and regulating the acrosome reaction. Variations in protein analyses and the protein contents and their abundances between animals contributed to the difficulty of establishing protein biomarkers of fertilizing potential of the bull sperm. Indeed, the heterogenicity of methodologies was a limitation of this review. Standardized methods of seminal protein analyses, as well as sperm endpoints, may minimize such discrepancies. In conclusion, potential biomarkers of sperm parameters are still to be established. Future studies should evaluate protein isoforms and how they interact with sperm to ascertain their biological functions.


1993 ◽  
Vol 64 (3) ◽  
pp. 221-227
Author(s):  
Soichi TSUJI ◽  
Masatoshi ASAO ◽  
Hiroshi KUSUNOKI ◽  
Takao OISHI

2021 ◽  
Vol 53 (1) ◽  
Author(s):  
Paula Lorena Souto ◽  
Lilian Silveira Travassos Carmouy ◽  
Cristiane Santos ◽  
Edison Martins ◽  
Vera Martins ◽  
...  

2000 ◽  
Vol 63 (5) ◽  
pp. 1531-1537 ◽  
Author(s):  
Beatriz Barrios ◽  
Rosaura Pérez-Pé ◽  
Margarita Gallego ◽  
Agustín Tato ◽  
Jesús Osada ◽  
...  

2007 ◽  
Vol 30 (12) ◽  
pp. 1979-1988 ◽  
Author(s):  
Md Imtaiyaz Hassan ◽  
Vijay Kumar ◽  
Tara Kashav ◽  
Neelima Alam ◽  
Tej P. Singh ◽  
...  

1998 ◽  
Vol 19 (5) ◽  
pp. 797-801 ◽  
Author(s):  
Michele Mortarino ◽  
Gabriella Tedeschi ◽  
Armando Negri ◽  
Fabrizio Ceciliani ◽  
Luciano Gottardi ◽  
...  

2009 ◽  
Vol 10 (1) ◽  
pp. 51 ◽  
Author(s):  
Jaime Antonio Cardozo ◽  
Patricia Grasa ◽  
María Teresa Muiño B. ◽  
José Álvaro Cebrián P.

<p>Este estudio se adelantó para evaluar el efecto de la adición de proteínas del plasma seminal de cordero en la criopreservación sobre la motilidad e integridad de la membrana espermática, y los cambios en el perfil electroforético de las proteínas de la membrana espermática inducidos por la criopreservación. Se usaron eyaculados de ocho corderos adultos de la raza rasa aragonesa, se les determinó su viabilidad y motilidad espermáticas y posteriormente se sometieron a un procedimiento de congelación. Las proteínas se separaron por el método de electroforesis en geles de acrilamida en dos dimensiones. Se obtuvo un mejoramiento significativo (<em>p </em>&lt; 0,05) en la calidad del semen congelado, cuando se adicionaron proteínas del plasma seminal. El análisis bidimensional comparativo entre el semen fresco y el congelado evidenció la pérdida de 8 puntos de proteína en el espermatozoide descongelado. La concentración de un punto de proteína de membrana espermática, de bajo peso molecular (punto 2), fue más alta (<em>p </em>&lt; 0,05) en el espermatozoide descongelado al que se adicionaron proteínas del plasma seminal. Se encontraron correlaciones entre algunos puntos de proteína y la motilidad y viabilidad espermáticas, lo cual sugiere que pueden jugar papeles importantes en el mantenimiento de la integridad y funcionalidad del espermatozoide. Se puede concluir que la adición de proteínas del plasma seminal en la congelación mejora la integridad del espermatozoide descongelado, y que la criopreservación del semen de cordero produce variaciones en la composición de las proteínas de membrana.  </p><p> </p><p><strong>Effect of seminal plasma proteins at freezing on ram sperm motility and viability</strong>  </p><p>The aim of the study was to evaluate the cryoprotective effect of seminal plasma proteins on ram sperm motility, membrane integrity and the changes in the profile of ram sperm membrane proteins induced by cryopreservation. Fresh ejaculates from 8 mature Rasa aragonesa rams were used. Sperm motility and cell viability was assessed. The freezing procedure was based on the method described by Fiser <em>et al</em>. (1987). Proteins extracted from fresh and frozen-thawed semen were subjected to the Two-dimensional polyacrilamide gel electrophoresis. A significant improvement in the quality of frozenthawed sperm was obtained after addition of seminal plasma proteins (<em>p </em>&lt; 0.05). Comparative two-dimensional polyacrilamide gel electrophoresis analysis between fresh and frozen semen, either with or without seminal plasma proteins in the cryopreservation medium, revealed that eight protein spots were lost in frozen-thawed sperm. The concentration of one sperm membrane protein spot of low Mr (spot 2) was higher (<em>p </em>&lt; 0.05) in proteinadded frozen sperm. Correlations found between certain protein spots sperm motility and viability suggests that these proteins could play important roles in the maintenance of sperm integrity and functionality. In conclusion, the addition of seminal plasma proteins to freezing extender improved frozen-thawed ram sperm integrity quality and cryopreservation of ram semen produced variations in the sperm membrane protein composition. </p>


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